It has been believed until only very recently that bacteria in general do not glycosylate their proteins. While there have been some instances reported, these were dismissed as unusual anomalies (Borman 2006). It is now becoming more accepted that bacteria do glycosylate their proteins in perhaps more ways than eukaryotes do, although this belief is not yet widespread (Schïffer et al., 2001). In a recent review article, it was stated that glycosylation has been shown to assist in protein stability, modulate physical properties such as solubility, protect against proteolysis, modify activity profiles, and target for externalization (Upreti et al., 2003). In 1994, a group purified an amylase from Alicyclobacillus acidocaldarius and showed that the amylase was cell-bound during active growth (Schwermann et al., 1994). As the culture entered stationary phase, the cells released an active soluble glycosylated version of the amylase into the medium (Schwermann et al., 1994). No attempt was made to compare the activities of the various forms of the amylases.